My sister is type A and is battling breast cancer. I am thinking of getting her some of the Helix product, but how do I explain to her why she should take it.

ANSWER:

Defects in surface glycosylation (the elaboration of long sugar chains) which in normal cells are very tightly restricted, is a characteristic of cancer cells. This results in the elaboration of tremendous amounts of glycoproteins, many of which (CA-125, CA15-3, CA 19-9, Lex) have clinical and diagnostic relevance. As neoplastic breast cells become malignantly competent, their surface glycosylation products alter, resulting in elaboration of structures characterized by the presence of GalNAc. It is the presence of these glycosylation products that allow for metastatic spread and poor prognosis. This molecule, an obscure ligand-like complex

(LLC) , is apparently absent from normal and early (non-metastatic) breast cancer cells. LLC can be considered a sort of "internal passport" for the breast cancer cells; allowing them free transit through the body. This complex shares many structural similarities with both A and M blood groups and may explain their particular succeptibility to breast cancer.

The common snail "Large Burgundy" contains a unique lectin called Helix pomatia agglutinin (HPA) which is capable of recognizing a ligand-like complex (LLC) elaborated as a surface glycosylation product on some tumor cells. Thus the consumption of this species of snail may serve as a very potent protective agent, as both these blood group antigens are associated with a higher risk of many of these cancers.

In 1987 and 1991 Brooks and co-workers (1, 2) reported that it is possible to predict lymph node involvement in women with breast cancer by the detection of altered glycosylation. Their 1991 study was performed on paraffin-embedded sections of 373 primary breast cancers, in a 24 year retrospective study, which were stained for the binding of Helix pomatia lectin. This lectin is nominally specific for N-acetyl-galactosamine (GalNAc). Brooks reported a strong association between HPA binding and the presence of lymph node metastases and proposed that HPA recognizes a glycoprotein associated with metastasis to axillary nodes and subsequent poor prognosis.

Springer (3) had earlier suggested that it may be related to the Tn blood group precursor substance, which is generally absent from normal tissue, yet detectable in a high proportion of breast cancer tissue. LLC also appears to display antigenic similarities to blood group A (the terminal antigen of which is GalNAc) and blood group M.

It has been shown that breast tumor cells which do not produce LLC tend to stay localized. These cells would not per se be susceptible to HPA agglutination. Interestingly, it would appear that HPA becomes active in an inverse ratio to tumor staging, i.e. as the malignancy worsens and LLC is increasingly elaborated, the tumor cells become paradoxically more susceptible to agglutination by HPA.